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R L Baehner

Publications and source records attributed to R L Baehner.

At least 217 records · Page 12Linked to original sources
PubMed1970

Respiration and glucose oxidation in human and guinea pig leukocytes: comparative studies.

A comparison has been made of the metabolic shifts in human and guinea pig leukocytes when they phagocytize. Respiration of guinea pig polymorphonuclear leukocytes (PMN) and the increment during phagocytosis were each about 2(1/2)-fold that of human PMN. This was also true of the direct oxidation of glucose-6-P (hexose monophosphate shunt). Enzymes potentially responsible for these phenomena have been compared in each species. Cyanide-insensitive NADH oxidase and NADPH oxidase were measured and only the formed exhibited adequate activity to account for the respiratory stimulus durintg phagocytosis. The hydrogen peroxide formed by this enzyme stimulates the hexose monophosphate shunt by oxidizing glutathione which upon reduction by an NADPH-linked glutathione reductase provides NADP to drive the hexose monophosphate shunt. Other linkages between respiratory stimulation and that of the hexose monophosphate shunt also pertain in the guinea pig.

Animals↗
PubMed1970

Correction of metabolic deficiencies in the leukocytes of patients with chronic granulomatous disease.

Polymorphonuclear leukocytes from patients with chronic granulomatous disease (CGD) exhibit metabolic and bactericidal deficiencies that may be the result of inadequate production of H(2)O(2). A hydrogen peroxide-generating system was, therefore, inserted into CGD leukocytes. This was accomplished by allowing the cells to phagocytize latex spherules coated with glucose oxidase. This produced an amelioration in the known metabolic deficiencies of these cells during phagocytosis: (a) intracellular (catalatic) formate oxidation dependent upon hydrogen peroxide production was enhanced fourfold; and (b) hexose monophosphate shunt activity, which other workers have shown to be at least partially dependent upon the availability of H(2)O(2), was markedly stimulated. These data strengthen the evidence that the fundamental metabolic lesion in CGD cells during phagocytosis is indeed deficient production of hydrogen peroxide, probably, as previously shown, due to diminished oxidase for reduced nicotinamide adenine dinucleotide.

Carbon Isotopes↗
PubMed1969

Degranulation of leukocytes in chronic granulomatous disease.

Quantitative chemical analyses of the subcellular distribution patterns for acid and alkaline phosphatase, beta glucuronidase and peroxidase were obtained for human peripheral blood leukocytes of four patients with chronic granulomatous disease (CGD). Five young adults with acute infections served as controls. The observations were made on fractions obtained by homogenization and centrifugation of leukocytes previously incubated with or without particles for ingestion. Distributions in resting CGD and normal cells were very similar for acid and alkaline phosphatase and peroxidase, but the proportion of beta glucuronidase in the granule fraction of CGD cells was depressed, with an increased proportion in the soluble fraction. Release of granule-bound enzymes during phagocytosis of a variety of particles was the same for CGD and control cells, except that release of beta glucuronidase was less marked in CGD cells. Total enzymatic activity of CGD cells for the hydrolases studied was normal. The data indicated that granular enzymes are released in a normal fashion in phagocytizing CGD cells. Supportive evidence of release of enzymes into the phagocytic vacuole of CGD cells was obtained by an electron microscopic study of myeloperoxidase.

Acid Phosphatase↗
PubMed1969

Failure of nitro blue tetrazolium reduction in the phagocytic vacuoles of leukocytes in chronic granulomatous disease.

The leukocytes of patients with chronic granulomatous disease (CGD) may be identified by their failure to reduce Nitro Blue Tetrazolium (NBT) during phagocytosis. This reaction, normally detected in the phagocytic vacuole, is absent or delayed in CGD monocytes and eosinophils as well as in neutrophils, even though sonicates of normal and CGD leukocytes contain equal activities of a cyanide insensitive enzyme system capable of reduction of NBT in the presence of pyridine nucleotide. Enlargement of CGD phagocytic vacuoles appears to be inhibited. Histochemical estimates of the rate of release of alkaline phosphatase are normal in CGD cells. Peroxidase activity is released from CGD cells, but the rate appears to be somewhat slower than normal in some cases. The latter observation may be explained by the increased intensity of the peroxidase stain in resting and phagocytizing CGD cells. The severity of the defect in NBT reduction within the phagocytic vacuoles of the leukocytes of patients and carriers is more variable than was previously appreciated. Some female carriers have profoundly reduced dye reduction and others are nearly indistinguishable from normal. Three brothers with CGD demonstrated significant, albeit delayed, NBT reduction in phagocytic vacuoles during prolonged incubation of their leukocytes. No obvious relationship exists, however, between the rate of reduction of NBT in vacuoles and the clinical severity of the disease.

Alkaline Phosphatase↗
PubMed1968

Deficiency of reduced nicotinamide-adenine dinucleotide oxidase in chronic granulomatous disease.

Reduced nicotinamide-adenine dinucleotide oxidase of normal human polymorphonuclear leukocytes has properties that would qualify it as the enzyme responsible for the respiratory burst during phagocytosis. The enzyme was deficient in leukocytes of five patients with chronic granulomatous disease. This lack of adequate reduced nicotinamide-adenine dinucleotide oxidase could be the basis for the metabolic abnormalities characteristic of these leukocytes and for their diminished bactericidal activity.

Blood Bactericidal Activity↗
PubMed1967

Leukocyte oxidase: defective activity in chronic granulomatous disease.

The intact leukocytes of two children with chronic granulomatous disease fail to reduce nitroblue tetrazolium during phagocytosis. This is due to defective operation of an oxidase of reduced nicotinamide adenine dinucleotide that is insensitive to cyanide and that indirectly stimulates the oxidation of glucose-6-phosphate in leukocytes. Such leukocytes undergo no increase in oxygen consumption or in activity of the hexose monophosphate shunt during phagocytosis, although lactate production is normal. The addition of nitroblue tetrazolium to a leukocyte suspension appears to provide a sensitive diagnostic screening test for this disease.

Carbon Isotopes↗